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- PDB-5adh: INTERDOMAIN MOTION IN LIVER ALCOHOL DEHYDROGENASE. STRUCTURAL AND... -
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Basic information
Entry | Database: PDB / ID: 5adh | |||||||||
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Title | INTERDOMAIN MOTION IN LIVER ALCOHOL DEHYDROGENASE. STRUCTURAL AND ENERGETIC ANALYSIS OF THE HINGE BENDING MODE | |||||||||
![]() | APO-LIVER ALCOHOL DEHYDROGENASE | |||||||||
![]() | OXIDOREDUCTASE (NAD(A)-CHOH(D)) | |||||||||
Function / homology | ![]() : / all-trans-retinol dehydrogenase (NAD+) activity / alcohol dehydrogenase / retinol metabolic process / retinoic acid metabolic process / zinc ion binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Eklund, H. / Jones, T.A. | |||||||||
![]() | ![]() Title: Interdomain motion in liver alcohol dehydrogenase. Structural and energetic analysis of the hinge bending mode. Authors: Colonna-Cesari, F. / Perahia, D. / Karplus, M. / Eklund, H. / Braden, C.I. / Tapia, O. #1: ![]() Title: Crystallographic Investigations of Nicotinamide Adenine Dinucleotide Binding to Horse Liver Alcohol Dehydrogenase Authors: Eklund, H. / Samama, J.-P. / Jones, T.A. #2: ![]() Title: Crystal Structures of the Active Site in Specifically Metal-Depleted and Cobalt-Substituted Horse Liver Alcohol Dehydrogenase Derivatives Authors: Schneider, G. / Eklund, H. / Cedergren-Zeppezauer, E. / Zeppezauer, M. #3: ![]() Title: Three-Dimensional Structure of Isonicotinimidylated Liver Alcohol Dehydrogenase Authors: Plapp, B.V. / Eklund, H. / Jones, T.A. / Branden, C.-I. #4: ![]() Title: Crystal-Structure Determination of Reduced Nicotinamide Adenine Dinucleotide Complex with Horse Liver Alcohol Dehydrogenase Maintained in its Apo Conformation by Zinc-Bound Imidazole Authors: Cedergren-Zeppezauer, E. #5: ![]() Title: Binding of Substrate in a Ternary Complex of Horse Liver Alcohol Dehydrogenase Authors: Eklund, H. / Plapp, B.V. / Samama, J.-P. / Branden, C.-I. #6: ![]() Title: Crystal Structure Determinations of Coenzyme Analogue and Substrate Complexes of Liver Alcohol Dehydrogeanse. Binding of 1,4,5,6-Tetrahydronicotinamide Adenine Dinucleotide and Trans-4-(N,N- ...Title: Crystal Structure Determinations of Coenzyme Analogue and Substrate Complexes of Liver Alcohol Dehydrogeanse. Binding of 1,4,5,6-Tetrahydronicotinamide Adenine Dinucleotide and Trans-4-(N,N-Dimethylamino)Cinnamaldehyde to the Enzyme Authors: Cedergren-Zeppezauer, E. / Samama, J.-P. / Eklund, H. #7: ![]() Title: Pyrazole Binding in Crystalline Binary and Ternary Complexes with Liver Alcohol Dehydrogenase Authors: Eklund, H. / Samama, J.-P. / Wallen, L. #8: ![]() Title: Structure of Triclinic Ternary Complex of Horse Liver Alcohol Dehydrogenase at 2.9 Angstroms Resolution Authors: Eklund, H. / Samama, J.-P. / Wallen, L. / Branden, C.-I. / Akeson, A. / Jones, T.A. #9: ![]() Title: 5-Methylnicotinamide-Adenine Dinucleotide. Kinetic Investigation with Major and Minor Isoenzymes of Liver Alcohol Dehydrogenase and Structural Determination of its Binary Complex with Alcohol Dehydrogenase Authors: Samama, J.-P. / Wrixon, A.D. / Biellmann, J.-F. #10: ![]() Title: Structural Differences between Apo-and Holoenzyme of Horse Liver Alcohol Dehydrogenase Authors: Eklund, H. / Branden, C.-I. #11: ![]() Title: X-Ray Studies of the Binding of Cibacron Blue F3Ga to Liver Alcohol Dehydrogenase Authors: Biellmann, J.-F. / Samama, J.-P. / Branden, C.I. / Eklund, H. #12: ![]() Title: Crystallography of Liver Alcohol Dehydrogenase Complexed with Substrates Authors: Plapp, B.V. / Eklund, H. / Branden, C.-I. #13: ![]() Title: Crystallization of Liver Alcohol Denydrogenase Activated by the Modification of Amino Groups Authors: Plapp, B.V. / Zeppezauer, E. / Branden, C.-I. #14: ![]() Title: Subunit Conformation of Yeast Alcohol Dehydrogenase Authors: Jornvall, H. / Eklund, H. / Branden, C.-I. #15: ![]() Title: The Crystal Structure of Complexes between Horse Liver Alcohol Dehydrogenase and the Coenzyme Analogues 3-Iodopyridine-Adenine Dinucleotide and Pyridine-Adenine Dinucleotide Authors: Samama, J.-P. / Zeppezauer, E. / Biellmann, J.-F. / Branden, C.-I. #16: ![]() Title: X-Ray Investigation of the Binding of 1,10-Phenanthroline and Imidazole to Horse-Liver Alcohol Dehydrogenase Authors: Boiwe, T. / Branden, C.-I. #17: ![]() Title: Three-Dimensional Structure of Horse Liver Alcohol Dehydrogenase at 2.4 Angstroms Resolution Authors: Eklund, H. / Nordstrom, B. / Zeppezauer, E. / Soderlund, G. / Ohlsson, I. / Boiwe, T. / Soderberg, B.-O. / Tapia, O. / Branden, C.-I. / Akeson, A. #18: ![]() Title: Structural Comparisons of Mammalian, Yeast and Bacillar Alcohol Dehydrogenases Authors: Eklund, H. / Branden, C.-I. / Jornvall, H. #19: ![]() Year: 1975 Title: The Binding of Nucleotides to Horse Liver Alcohol Dehydrogenase Authors: Nordstrom, B. / Branden, C.-I. #20: ![]() Title: Alcohol Dehydrogenases Authors: Branden, C.-I. / Jornvall, H. / Eklund, H. / Furugren, B. #21: ![]() Title: The Conformation of Adenosine Diphosphoribose and 8-Bromoadenosine Diphosphoribose When Bound to Liver Alcohol Dehydrogenase Authors: Abdallah, M.A. / Biellmann, J.-F. / Nordstrom, B. / Branden, C.-I. #22: ![]() Title: The Structure of Horse Liver Alcohol Dehydrogenase Authors: Eklund, H. / Nordstrom, B. / Zeppezauer, E. / Soderlund, G. / Ohlsson, I. / Boiwe, T. / Branden, C.-I. #23: ![]() Title: Structural and Functional Similarities within the Coenzyme Binding Domains of Dehydrogenases Authors: Ohlsson, I. / Nordstrom, B. / Branden, C.-I. #24: ![]() Title: Binding of Salicylate in the Adenosine-Binding Pocket of Dehydrogenases Authors: Einarsson, R. / Eklund, H. / Zeppezauer, E. / Boiwe, T. / Branden, C.-I. #25: ![]() Title: Structure of Liver Alcohol Dehydrogenase at 2.9-Angstroms Resolution Authors: Branden, C.-I. / Eklund, H. / Nordstrom, B. / Boiwe, T. / Soderlund, G. / Zeppezauer, E. / Ohlsson, I. / Akeson, A. #26: ![]() Title: Structure of Horse Liver Alcohol Dehydrogenase. I. Structural Symmetry and Conformational Changes Authors: Branden, C.-I. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 84.9 KB | Display | ![]() |
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PDB format | ![]() | 60.9 KB | Display | ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Atom site foot note | 1: RESIDUE 62 IS A CIS-PROLINE. 2: THIS ATOM WAS NOT LOCATED IN THE ELECTRON DENSITY MAP. COORDINATES WERE GENERATED USING STEREOCHEMICAL CRITERIA. | ||||||||
Components on special symmetry positions |
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Components
#1: Protein | Mass: 39853.273 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() | ||||||
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#2: Chemical | #3: Chemical | ChemComp-APR / | #4: Chemical | ChemComp-MPD / ( | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48.72 % |
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Crystal grow | *PLUS Method: unknown |
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Processing
Refinement | Highest resolution: 2.9 Å | ||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 2.9 Å
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